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Conserved domains on  [gi|213021190|ref|NP_001132940|]
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F-box-like/WD repeat-containing protein TBL1X isoform b [Homo sapiens]

Protein Classification

WD40 domain-containing protein( domain architecture ID 10553538)

WD40 domain-containing protein similar to Homo sapiens F-box-like/WD repeat-containing protein TBL1X/TBL1Y/TBL1XR1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 176-482 7.61e-87

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


:

Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 269.59  E-value: 7.61e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 176 VLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLNENsnggstqlvlRHCIREGGHDVPsnkdVTSLDWNTNGTLLATG 255
Cdd:cd00200    4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETG----------ELLRTLKGHTGP----VRDVAASADGTYLASG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 256 SYDGFARIW-TEDGNLASTLGQHKGPIFALKWNRKGNYILSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDWQNNTTF 334
Cdd:cd00200   70 SSDKTIRLWdLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTF 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 335 -ASCSTDMCIHVCRLGCDRPVKTFQGHTNEVNAIKWDPSGMLLASCSDDMTLKIWSMKQEVCIHDLQAHNKEIYTIKWSP 413
Cdd:cd00200  150 vASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSP 229

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 213021190 414 tgpatsnpnSNIMLASASFDSTVRLWDIERGVCTHTLTKHQEPVYSVAFSPDGKYLASGSFDKCVHIWN 482
Cdd:cd00200  230 ---------DGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
 7-31 5.75e-07

LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The LisH domain is found in Sif2, a component of the Set3 complex which is responsible for repressing meiotic genes. It has been shown that the LisH domain helps mediate interaction with components of the Set3 complex.


:

Pssm-ID: 462501  Cd Length: 25  Bit Score: 45.77  E-value: 5.75e-07
                          10        20
                  ....*....|....*....|....*
gi 213021190    7 EVNFLVYRYLQESGFSHSAFTFGIE 31
Cdd:pfam08513   1 ELNRLIYDYLVKEGYEETAEAFEKE 25
8prop_heme_binding_protein super family cl49617
eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; ...
 456-526 6.61e-04

eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; Members here contain an 8-bladed beta-propeller heme-binding domain in cytochrome cd1 (nitrite reductase) and similar proteins including NirN and NirF. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO(3-)-> NO(2-)-> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic nitrite reductase NirS via its maturation factor NirF. NirN and NirF form a stable complex with the nitrite reductase NirS during enzyme maturation. NirF is involved in heme d1 insertion.


The actual alignment was detected with superfamily member cd20778:

Pssm-ID: 483957 [Multi-domain]  Cd Length: 381  Bit Score: 42.27  E-value: 6.61e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 213021190 456 PVYSVAfSPDGKYLA---SGSFDKCVHIWNTQSGNLVHSYRGTGGIFEVCWNARGDKVGASASDGS-VCVLDLRK 526
Cdd:cd20778  283 PVFAVA-RPDGRYVWvnfSGPDNDTVQVIDTKTLKVVKTLEPGKRVLHMEFTPRGEAVYISVNDDNkVVVYDTRT 356
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 176-482 7.61e-87

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 269.59  E-value: 7.61e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 176 VLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLNENsnggstqlvlRHCIREGGHDVPsnkdVTSLDWNTNGTLLATG 255
Cdd:cd00200    4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETG----------ELLRTLKGHTGP----VRDVAASADGTYLASG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 256 SYDGFARIW-TEDGNLASTLGQHKGPIFALKWNRKGNYILSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDWQNNTTF 334
Cdd:cd00200   70 SSDKTIRLWdLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTF 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 335 -ASCSTDMCIHVCRLGCDRPVKTFQGHTNEVNAIKWDPSGMLLASCSDDMTLKIWSMKQEVCIHDLQAHNKEIYTIKWSP 413
Cdd:cd00200  150 vASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSP 229

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 213021190 414 tgpatsnpnSNIMLASASFDSTVRLWDIERGVCTHTLTKHQEPVYSVAFSPDGKYLASGSFDKCVHIWN 482
Cdd:cd00200  230 ---------DGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
174-525 1.45e-79

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 254.45  E-value: 1.45e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 174 ATVLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLNensnGGSTQLVLRhciregGHDvpsnKDVTSLDWNTNGTLLA 253
Cdd:COG2319   71 LATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLA----TGLLLRTLT------GHT----GAVRSVAFSPDGKTLA 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 254 TGSYDGFARIW-TEDGNLASTLGQHKGPIFALKWNRKGNYILSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDW-QNN 331
Cdd:COG2319  137 SGSADGTVRLWdLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFsPDG 216

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 332 TTFASCSTDMCIHVCRLGCDRPVKTFQGHTNEVNAIKWDPSGMLLASCSDDMTLKIWSMKQEVCIHDLQAHNKEIYTIKW 411
Cdd:COG2319  217 KLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAF 296

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 412 SPTGPatsnpnsniMLASASFDSTVRLWDIERGVCTHTLTKHQEPVYSVAFSPDGKYLASGSFDKCVHIWNTQSGNLVHS 491
Cdd:COG2319  297 SPDGK---------LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRT 367

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 213021190 492 YRG-TGGIFEVCWNARGDKVGASASDGSVCVLDLR 525
Cdd:COG2319  368 LTGhTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
PTZ00420 PTZ00420
coronin; Provisional
 353-442 1.37e-11

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 66.90  E-value: 1.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 353 PVKTFQGHTNEVNAIKWDPS-GMLLASCSDDMTLKIWSMKQE----------VCIhdLQAHNKEIYTIKWsptgpatsNP 421
Cdd:PTZ00420  66 PVIKLKGHTSSILDLQFNPCfSEILASGSEDLTIRVWEIPHNdesvkeikdpQCI--LKGHKKKISIIDW--------NP 135

                         90       100
                 ....*....|....*....|.
gi 213021190 422 NSNIMLASASFDSTVRLWDIE 442
Cdd:PTZ00420 136 MNYYIMCSSGFDSFVNIWDIE 156
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 444-482 1.49e-10

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 56.17  E-value: 1.49e-10
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 213021190   444 GVCTHTLTKHQEPVYSVAFSPDGKYLASGSFDKCVHIWN 482
Cdd:smart00320   2 GELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
444-482 4.85e-10

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 54.66  E-value: 4.85e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 213021190  444 GVCTHTLTKHQEPVYSVAFSPDGKYLASGSFDKCVHIWN 482
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
 7-31 5.75e-07

LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The LisH domain is found in Sif2, a component of the Set3 complex which is responsible for repressing meiotic genes. It has been shown that the LisH domain helps mediate interaction with components of the Set3 complex.


Pssm-ID: 462501  Cd Length: 25  Bit Score: 45.77  E-value: 5.75e-07
                          10        20
                  ....*....|....*....|....*
gi 213021190    7 EVNFLVYRYLQESGFSHSAFTFGIE 31
Cdd:pfam08513   1 ELNRLIYDYLVKEGYEETAEAFEKE 25
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 7-36 1.45e-05

Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly.


Pssm-ID: 128913  Cd Length: 34  Bit Score: 42.04  E-value: 1.45e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 213021190     7 EVNFLVYRYLQESGFSHSAFTFGIESHISQ 36
Cdd:smart00667   5 ELNRLILEYLLRNGYEETAETLQKESGLSL 34
8prop_hemeD1_NirF cd20778
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ...
 456-526 6.61e-04

eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; Denitrification is a process that enables biofilm formation of the opportunistic human pathogen Pseudomonas aeruginosa, making it more resilient to antibiotics and highly adaptable to different habitats. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO3- -> NO2- -> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic cytochrome cd1 (nitrite reductase) NirS via its maturation factor NirF. The nirFDLGHJE genes encode proteins required for heme d1 biosynthesis. NirS, NirF, and NirN, the monomeric dihydro-heme d1 dehydrogenase form a stable complex during nitrite reductase maturation. The nitrite reductase NirS is bound to the denitrification supercomplex via NorB, while the electron donor system NirM and the enzyme maturation machinery NirN-NirF-NirQ, interacting with NirS, are bound via NorC.


Pssm-ID: 467722 [Multi-domain]  Cd Length: 381  Bit Score: 42.27  E-value: 6.61e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 213021190 456 PVYSVAfSPDGKYLA---SGSFDKCVHIWNTQSGNLVHSYRGTGGIFEVCWNARGDKVGASASDGS-VCVLDLRK 526
Cdd:cd20778  283 PVFAVA-RPDGRYVWvnfSGPDNDTVQVIDTKTLKVVKTLEPGKRVLHMEFTPRGEAVYISVNDDNkVVVYDTRT 356
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 176-482 7.61e-87

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 269.59  E-value: 7.61e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 176 VLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLNENsnggstqlvlRHCIREGGHDVPsnkdVTSLDWNTNGTLLATG 255
Cdd:cd00200    4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETG----------ELLRTLKGHTGP----VRDVAASADGTYLASG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 256 SYDGFARIW-TEDGNLASTLGQHKGPIFALKWNRKGNYILSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDWQNNTTF 334
Cdd:cd00200   70 SSDKTIRLWdLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTF 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 335 -ASCSTDMCIHVCRLGCDRPVKTFQGHTNEVNAIKWDPSGMLLASCSDDMTLKIWSMKQEVCIHDLQAHNKEIYTIKWSP 413
Cdd:cd00200  150 vASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSP 229

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 213021190 414 tgpatsnpnSNIMLASASFDSTVRLWDIERGVCTHTLTKHQEPVYSVAFSPDGKYLASGSFDKCVHIWN 482
Cdd:cd00200  230 ---------DGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
174-525 1.45e-79

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 254.45  E-value: 1.45e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 174 ATVLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLNensnGGSTQLVLRhciregGHDvpsnKDVTSLDWNTNGTLLA 253
Cdd:COG2319   71 LATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLA----TGLLLRTLT------GHT----GAVRSVAFSPDGKTLA 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 254 TGSYDGFARIW-TEDGNLASTLGQHKGPIFALKWNRKGNYILSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDW-QNN 331
Cdd:COG2319  137 SGSADGTVRLWdLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFsPDG 216

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 332 TTFASCSTDMCIHVCRLGCDRPVKTFQGHTNEVNAIKWDPSGMLLASCSDDMTLKIWSMKQEVCIHDLQAHNKEIYTIKW 411
Cdd:COG2319  217 KLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAF 296

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 412 SPTGPatsnpnsniMLASASFDSTVRLWDIERGVCTHTLTKHQEPVYSVAFSPDGKYLASGSFDKCVHIWNTQSGNLVHS 491
Cdd:COG2319  297 SPDGK---------LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRT 367

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 213021190 492 YRG-TGGIFEVCWNARGDKVGASASDGSVCVLDLR 525
Cdd:COG2319  368 LTGhTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 COG2319
WD40 repeat [General function prediction only];
174-485 2.41e-79

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 254.07  E-value: 2.41e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 174 ATVLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLNensnGGSTQLVLRhciregGHDvpsnKDVTSLDWNTNGTLLA 253
Cdd:COG2319  113 LRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLA----TGKLLRTLT------GHS----GAVTSVAFSPDGKLLA 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 254 TGSYDGFARIW-TEDGNLASTLGQHKGPIFALKWNRKGNYILSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDW-QNN 331
Cdd:COG2319  179 SGSDDGTVRLWdLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFsPDG 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 332 TTFASCSTDMCIHVCRLGCDRPVKTFQGHTNEVNAIKWDPSGMLLASCSDDMTLKIWSMKQEVCIHDLQAHNKEIYTIKW 411
Cdd:COG2319  259 RLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAF 338

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 213021190 412 SPTGPatsnpnsniMLASASFDSTVRLWDIERGVCTHTLTKHQEPVYSVAFSPDGKYLASGSFDKCVHIWNTQS 485
Cdd:COG2319  339 SPDGK---------TLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
174-525 3.80e-61

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 206.30  E-value: 3.80e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 174 ATVLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLNensnGGSTQLVLRhciregGHDVPsnkdVTSLDWNTNGTLLA 253
Cdd:COG2319   29 LLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAA----AGALLATLL------GHTAA----VLSVAFSPDGRLLA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 254 TGSYDGFARIW-TEDGNLASTLGQHKGPIFALKWNRKGNYILSAGVDKTTIIWDAHTGeakqqfpfhsapaldvdwqnnt 332
Cdd:COG2319   95 SASADGTVRLWdLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATG---------------------- 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 333 tfascstdmcihvcrlgcdRPVKTFQGHTNEVNAIKWDPSGMLLASCSDDMTLKIWSMKQEVCIHDLQAHNKEIYTIKWS 412
Cdd:COG2319  153 -------------------KLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFS 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 413 PTGPatsnpnsniMLASASFDSTVRLWDIERGVCTHTLTKHQEPVYSVAFSPDGKYLASGSFDKCVHIWNTQSGNLVHSY 492
Cdd:COG2319  214 PDGK---------LLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTL 284

                        330       340       350
                 ....*....|....*....|....*....|....
gi 213021190 493 RG-TGGIFEVCWNARGDKVGASASDGSVCVLDLR 525
Cdd:COG2319  285 TGhSGGVNSVAFSPDGKLLASGSDDGTVRLWDLA 318
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 270-526 6.36e-61

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 202.18  E-value: 6.36e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 270 LASTLGQHKGPIFALKWNRKGNYILSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDW-QNNTTFASCSTDMCIHVCRL 348
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAAsADGTYLASGSSDKTIRLWDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 349 GCDRPVKTFQGHTNEVNAIKWDPSGMLLASCSDDMTLKIWSMKQEVCIHDLQAHNKEIYTIKWSPTgpatsnpnsNIMLA 428
Cdd:cd00200   81 ETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPD---------GTFVA 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 429 SASFDSTVRLWDIERGVCTHTLTKHQEPVYSVAFSPDGKYLASGSFDKCVHIWNTQSGNLVHSYRG-TGGIFEVCWNARG 507
Cdd:cd00200  152 SSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGhENGVNSVAFSPDG 231

                        250
                 ....*....|....*....
gi 213021190 508 DKVGASASDGSVCVLDLRK 526
Cdd:cd00200  232 YLLASGSEDGTIRVWDLRT 250
WD40 COG2319
WD40 repeat [General function prediction only];
250-525 1.12e-50

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 178.57  E-value: 1.12e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 250 TLLATGSYDGFARIWTEDGNLASTLGQHKGPIFALKWNRKGNYILSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDWQ 329
Cdd:COG2319    8 ALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFS 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 330 -NNTTFASCSTDMCIHVCRLGCDRPVKTFQGHTNEVNAIKWDPSGMLLASCSDDMTLKIWSMKQEVCIHDLQAHNKEIYT 408
Cdd:COG2319   88 pDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTS 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 409 IKWSPTGPatsnpnsniMLASASFDSTVRLWDIERGVCTHTLTKHQEPVYSVAFSPDGKYLASGSFDKCVHIWNTQSGNL 488
Cdd:COG2319  168 VAFSPDGK---------LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKL 238

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 213021190 489 VHSYRG-TGGIFEVCWNARGDKVgASAS-DGSVCVLDLR 525
Cdd:COG2319  239 LRTLTGhSGSVRSVAFSPDGRLL-ASGSaDGTVRLWDLA 276
PTZ00420 PTZ00420
coronin; Provisional
 353-442 1.37e-11

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 66.90  E-value: 1.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 353 PVKTFQGHTNEVNAIKWDPS-GMLLASCSDDMTLKIWSMKQE----------VCIhdLQAHNKEIYTIKWsptgpatsNP 421
Cdd:PTZ00420  66 PVIKLKGHTSSILDLQFNPCfSEILASGSEDLTIRVWEIPHNdesvkeikdpQCI--LKGHKKKISIIDW--------NP 135

                         90       100
                 ....*....|....*....|.
gi 213021190 422 NSNIMLASASFDSTVRLWDIE 442
Cdd:PTZ00420 136 MNYYIMCSSGFDSFVNIWDIE 156
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 444-482 1.49e-10

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 56.17  E-value: 1.49e-10
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 213021190   444 GVCTHTLTKHQEPVYSVAFSPDGKYLASGSFDKCVHIWN 482
Cdd:smart00320   2 GELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PTZ00420 PTZ00420
coronin; Provisional
 177-320 2.15e-10

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 63.05  E-value: 2.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 177 LRGHESEVFICAWNPV-SDLLASGSGDSTARIWNLNENSNgGSTQLVLRHCIREGghdvpSNKDVTSLDWN-TNGTLLAT 254
Cdd:PTZ00420  70 LKGHTSSILDLQFNPCfSEILASGSEDLTIRVWEIPHNDE-SVKEIKDPQCILKG-----HKKKISIIDWNpMNYYIMCS 143

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 213021190 255 GSYDGFARIW-TEDGNLASTLGQHKgPIFALKWNRKGNYILSAGVDKTTIIWDAHTGEAKQQFPFHS 320
Cdd:PTZ00420 144 SGFDSFVNIWdIENEKRAFQINMPK-KLSSLKWNIKGNLLSGTCVGKHMHIIDPRKQEIASSFHIHD 209
WD40 pfam00400
WD domain, G-beta repeat;
444-482 4.85e-10

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 54.66  E-value: 4.85e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 213021190  444 GVCTHTLTKHQEPVYSVAFSPDGKYLASGSFDKCVHIWN 482
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 352-389 9.20e-10

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 53.86  E-value: 9.20e-10
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 213021190   352 RPVKTFQGHTNEVNAIKWDPSGMLLASCSDDMTLKIWS 389
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PTZ00421 PTZ00421
coronin; Provisional
 359-491 5.38e-09

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 58.37  E-value: 5.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 359 GHTNEVNAIKWDP-SGMLLASCSDDMTLKIWSMKQEVC-------IHDLQAHNKEIytikwsptGPATSNPNSNIMLASA 430
Cdd:PTZ00421  73 GQEGPIIDVAFNPfDPQKLFTASEDGTIMGWGIPEEGLtqnisdpIVHLQGHTKKV--------GIVSFHPSAMNVLASA 144

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 213021190 431 SFDSTVRLWDIERGVCTHTLTKHQEPVYSVAFSPDGKYLASGSFDKCVHIWNTQSGNLVHS 491
Cdd:PTZ00421 145 GADMVVNVWDVERGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRDGTIVSS 205
WD40 pfam00400
WD domain, G-beta repeat;
352-389 5.87e-09

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 51.58  E-value: 5.87e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 213021190  352 RPVKTFQGHTNEVNAIKWDPSGMLLASCSDDMTLKIWS 389
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
 7-31 5.75e-07

LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The LisH domain is found in Sif2, a component of the Set3 complex which is responsible for repressing meiotic genes. It has been shown that the LisH domain helps mediate interaction with components of the Set3 complex.


Pssm-ID: 462501  Cd Length: 25  Bit Score: 45.77  E-value: 5.75e-07
                          10        20
                  ....*....|....*....|....*
gi 213021190    7 EVNFLVYRYLQESGFSHSAFTFGIE 31
Cdd:pfam08513   1 ELNRLIYDYLVKEGYEETAEAFEKE 25
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 361-525 6.93e-07

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 52.01  E-value: 6.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 361 TNEVNAIKWDPSGMLLASCSDDMTLKIWS----MKQEVCIH----DLQAHNKeIYTIKWsptgpatsnpNSNI--MLASA 430
Cdd:PLN00181 483 SNLVCAIGFDRDGEFFATAGVNKKIKIFEcesiIKDGRDIHypvvELASRSK-LSGICW----------NSYIksQVASS 551

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 431 SFDSTVRLWDIERGVCTHTLTKHQEPVYSVAF-SPDGKYLASGSFDKCVHIWNTQSGNLVHSYRGTGGIFEVCW-NARGD 508
Cdd:PLN00181 552 NFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYsSADPTLLASGSDDGSVKLWSINQGVSIGTIKTKANICCVQFpSESGR 631

                        170
                 ....*....|....*..
gi 213021190 509 KVGASASDGSVCVLDLR 525
Cdd:PLN00181 632 SLAFGSADHKVYYYDLR 648
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 283-524 8.24e-07

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 52.01  E-value: 8.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 283 ALKWNRKGNYILSAGVDKTTIIWDAHTgEAKQQFPFHSaPALDVD---------WQN--NTTFASCSTDMCIHVCRLGCD 351
Cdd:PLN00181 488 AIGFDRDGEFFATAGVNKKIKIFECES-IIKDGRDIHY-PVVELAsrsklsgicWNSyiKSQVASSNFEGVVQVWDVARS 565

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 352 RPVKTFQGHTNEVNAIKW---DPSgmLLASCSDDMTLKIWSMKQEVCIHDLQAhNKEIYTIKW-SPTGPATS-------- 419
Cdd:PLN00181 566 QLVTEMKEHEKRVWSIDYssaDPT--LLASGSDDGSVKLWSINQGVSIGTIKT-KANICCVQFpSESGRSLAfgsadhkv 642

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 420 ------NPN-------------------SNIMLASASFDSTVRLWDIERGVC------THTLTKHQEPVYSVAFSPDGKY 468
Cdd:PLN00181 643 yyydlrNPKlplctmighsktvsyvrfvDSSTLVSSSTDNTLKLWDLSMSISginetpLHSFMGHTNVKNFVGLSVSDGY 722

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 469 LASGSFDKCVHIWNTQSGNLVHSYR--------------GTGGIFEVCWNARGDKVGASASDGSVCVLDL 524
Cdd:PLN00181 723 IATGSETNEVFVYHKAFPMPVLSYKfktidpvsglevddASQFISSVCWRGQSSTLVAANSTGNIKILEM 792
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 176-209 2.83e-06

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 44.23  E-value: 2.83e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 213021190   176 VLRGHESEVFICAWNPVSDLLASGSGDSTARIWN 209
Cdd:smart00320   7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 395-440 4.36e-06

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 43.46  E-value: 4.36e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 213021190   395 CIHDLQAHNKEIYTIKWSPTGPatsnpnsniMLASASFDSTVRLWD 440
Cdd:smart00320   4 LLKTLKGHTGPVTSVAFSPDGK---------YLASGSDDGTIKLWD 40
eIF2A pfam08662
Eukaryotic translation initiation factor eIF2A; This is a family of eukaryotic translation ...
 284-492 6.36e-06

Eukaryotic translation initiation factor eIF2A; This is a family of eukaryotic translation initiation factors.


Pssm-ID: 462552 [Multi-domain]  Cd Length: 194  Bit Score: 46.88  E-value: 6.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190  284 LKWNRKGNYIL---SAGVDKTTIIWdahTGEakqqfpfhsapaldvdwqnnTTFASCSTDMcIHVCRLGCDRpvktfqgh 360
Cdd:pfam08662  11 LKWNKNGTYLLvltDTDVDKTGKSY---YGE--------------------TNLYLIGETG-GPDCVVELDK-------- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190  361 TNEVNAIKWDPSGMLLASCSDDMTLKI--WSMKQEVcIHDLQAHNKEiyTIKWSPTGPatsnpnsniMLASASFDST--- 435
Cdd:pfam08662  59 EGPIHDVAWSPNGKEFAVIYGYMPAKVsfFDLKGNV-IHSFGEQPRN--TIFWSPFGR---------LVLLAGFGNLagd 126

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 213021190  436 VRLWDIERGVCTHTlTKHQEPVYsVAFSPDGKYLASGS------FDKCVHIWnTQSGNLVHSY 492
Cdd:pfam08662 127 IEFWDVVNKKKIAT-AEASNATL-CEWSPDGRYFLTATtaprlrVDNGFKIW-HYNGALVYKY 186
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 7-36 1.45e-05

Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly.


Pssm-ID: 128913  Cd Length: 34  Bit Score: 42.04  E-value: 1.45e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 213021190     7 EVNFLVYRYLQESGFSHSAFTFGIESHISQ 36
Cdd:smart00667   5 ELNRLILEYLLRNGYEETAETLQKESGLSL 34
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 267-306 1.72e-05

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 41.91  E-value: 1.72e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 213021190   267 DGNLASTLGQHKGPIFALKWNRKGNYILSAGVDKTTIIWD 306
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
175-209 1.89e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 41.56  E-value: 1.89e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 213021190  175 TVLRGHESEVFICAWNPVSDLLASGSGDSTARIWN 209
Cdd:pfam00400   5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
395-440 2.37e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 41.56  E-value: 2.37e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 213021190  395 CIHDLQAHNKEIYTIKWSPTGPatsnpnsniMLASASFDSTVRLWD 440
Cdd:pfam00400   3 LLKTLEGHTGSVTSLAFSPDGK---------LLASGSDDGTVKVWD 39
PTZ00421 PTZ00421
coronin; Provisional
 171-334 2.97e-05

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 46.42  E-value: 2.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 171 SSKATVLRGHESEVFICAWNP-VSDLLASGSGDSTARIWNLNEnsnGGSTQLVLRHciregghdvpsNKDVTSLDWNTNG 249
Cdd:PTZ00421 115 SDPIVHLQGHTKKVGIVSFHPsAMNVLASAGADMVVNVWDVER---GKAVEVIKCH-----------SDQITSLEWNLDG 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 250 TLLATGSYDGFARIWT-EDGNLASTLGQHKGPIFA-LKWNRKGNYILSAGVDKT----TIIWDAHTGEAkqqfPFHSapa 323
Cdd:PTZ00421 181 SLLCTTSKDKKLNIIDpRDGTIVSSVEAHASAKSQrCLWAKRKDLIITLGCSKSqqrqIMLWDTRKMAS----PYST--- 253

                        170
                 ....*....|.
gi 213021190 324 LDVDwQNNTTF 334
Cdd:PTZ00421 254 VDLD-QSSALF 263
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 363-470 1.46e-04

Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown];


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 44.64  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190  363 EVNAIKWDPSGMLLASCSDDMTLKIWSMK----QEVcihDLQAHNKEIYTIKWSPTGP--ATSNPNSNIMlasasfdSTV 436
Cdd:COG4946   390 RVFNPVWSPDGKKIAFTDNRGRLWVVDLAsgkvRKV---DTDGYGDGISDLAWSPDSKwlAYSKPGPNQL-------SQI 459

                          90       100       110
                  ....*....|....*....|....*....|....
gi 213021190  437 RLWDIERGVcTHTLTKHQEPVYSVAFSPDGKYLA 470
Cdd:COG4946   460 FLYDVETGK-TVQLTDGRYDDGSPAFSPDGKYLY 492
WD40 pfam00400
WD domain, G-beta repeat;
268-306 1.56e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 39.25  E-value: 1.56e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 213021190  268 GNLASTLGQHKGPIFALKWNRKGNYILSAGVDKTTIIWD 306
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 237-264 1.65e-04

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 39.22  E-value: 1.65e-04
                           10        20
                   ....*....|....*....|....*...
gi 213021190   237 NKDVTSLDWNTNGTLLATGSYDGFARIW 264
Cdd:smart00320  12 TGPVTSVAFSPDGKYLASGSDDGTIKLW 39
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
401-524 1.81e-04

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 43.14  E-value: 1.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 401 AHNKEIYTIK--WSPTGPATSnPNSNIMLASASFDSTVRLWDIERGVCTHTLTKHQEPvYSVAFSPDGKYL-----ASGS 473
Cdd:COG3391   98 ATGKVVATIPvgGGPRGLAVD-PDGGRLYVADSGNGRVSVIDTATGKVVATIPVGAGP-HGIAVDPDGKRLyvansGSNT 175

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 213021190 474 FDKCVHIWNTQSGNLVHSYRGTGGIFEVCWNARGDKV--------GASASDGSVCVLDL 524
Cdd:COG3391  176 VSVIVSVIDTATGKVVATIPVGGGPVGVAVSPDGRRLyvanrgsnTSNGGSNTVSVIDL 234
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 188-287 3.10e-04

Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC,


Pssm-ID: 403945 [Multi-domain]  Cd Length: 91  Bit Score: 39.95  E-value: 3.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190  188 AWNPVSDLLASGSGD--------STARIWNLNENSNGGStqlvlrhciregghdvpsnkdVTSLDWNTNGTLLATGSYDG 259
Cdd:pfam12894   2 SWCPTMDLIALATEDgelllhrlNWQRVWTLSPDKEDLE---------------------VTSLAWRPDGKLLAVGYSDG 60

                          90       100
                  ....*....|....*....|....*....
gi 213021190  260 FARIW-TEDGNLASTLGQHKGPIFALKWN 287
Cdd:pfam12894  61 TVRLLdAENGKIVHHFSAGSDLITCLGWG 89
WD40 pfam00400
WD domain, G-beta repeat;
237-264 3.21e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 38.10  E-value: 3.21e-04
                          10        20
                  ....*....|....*....|....*...
gi 213021190  237 NKDVTSLDWNTNGTLLATGSYDGFARIW 264
Cdd:pfam00400  11 TGSVTSLAFSPDGKLLASGSDDGTVKVW 38
8prop_hemeD1_NirF cd20778
eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; ...
 456-526 6.61e-04

eight-bladed heme d1-binding beta-propeller domain in cytochrome cd1 nitrate reductase NirF; Denitrification is a process that enables biofilm formation of the opportunistic human pathogen Pseudomonas aeruginosa, making it more resilient to antibiotics and highly adaptable to different habitats. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO3- -> NO2- -> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic cytochrome cd1 (nitrite reductase) NirS via its maturation factor NirF. The nirFDLGHJE genes encode proteins required for heme d1 biosynthesis. NirS, NirF, and NirN, the monomeric dihydro-heme d1 dehydrogenase form a stable complex during nitrite reductase maturation. The nitrite reductase NirS is bound to the denitrification supercomplex via NorB, while the electron donor system NirM and the enzyme maturation machinery NirN-NirF-NirQ, interacting with NirS, are bound via NorC.


Pssm-ID: 467722 [Multi-domain]  Cd Length: 381  Bit Score: 42.27  E-value: 6.61e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 213021190 456 PVYSVAfSPDGKYLA---SGSFDKCVHIWNTQSGNLVHSYRGTGGIFEVCWNARGDKVGASASDGS-VCVLDLRK 526
Cdd:cd20778  283 PVFAVA-RPDGRYVWvnfSGPDNDTVQVIDTKTLKVVKTLEPGKRVLHMEFTPRGEAVYISVNDDNkVVVYDTRT 356
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 338-412 1.03e-03

Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC,


Pssm-ID: 403945 [Multi-domain]  Cd Length: 91  Bit Score: 38.41  E-value: 1.03e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 213021190  338 STDMCIHVCRLGCDRPVKTFQ-GHTNEVNAIKWDPSGMLLASCSDDMTLKIWSMKQEVCIHDLQAHNKEIYTIKWS 412
Cdd:pfam12894  14 TEDGELLLHRLNWQRVWTLSPdKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSAGSDLITCLGWG 89
PTZ00420 PTZ00420
coronin; Provisional
 176-306 1.11e-03

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 41.47  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190 176 VLRGHESEVFICAWNPVSDLLASGSG-DSTARIWNL-NENSnggSTQLVLrhciregghdvpsNKDVTSLDWNTNGTLLa 253
Cdd:PTZ00420 120 ILKGHKKKISIIDWNPMNYYIMCSSGfDSFVNIWDIeNEKR---AFQINM-------------PKKLSSLKWNIKGNLL- 182

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 213021190 254 TGSYDG--FARIWTEDGNLASTLGQHKGP-----IFALKWNRKGNYILSAGVDKTTI----IWD 306
Cdd:PTZ00420 183 SGTCVGkhMHIIDPRKQEIASSFHIHDGGkntknIWIDGLGGDDNYILSTGFSKNNMremkLWD 246
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 437-504 2.32e-03

Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC,


Pssm-ID: 403945 [Multi-domain]  Cd Length: 91  Bit Score: 37.26  E-value: 2.32e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 213021190  437 RLWDIergvcthTLTKHQEPVYSVAFSPDGKYLASGSFDKCVHIWNTQSGNLVHSYR-GTGGIFEVCWN 504
Cdd:pfam12894  28 RVWTL-------SPDKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSaGSDLITCLGWG 89
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 243-331 8.51e-03

Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC,


Pssm-ID: 403945 [Multi-domain]  Cd Length: 91  Bit Score: 35.72  E-value: 8.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213021190  243 LDWNTNGTLLATGSYDG--------FARIWTEDGnlastlGQHKGPIFALKWNRKGNYILSAGVDKTTIIWDAHTGEAKQ 314
Cdd:pfam12894   1 MSWCPTMDLIALATEDGelllhrlnWQRVWTLSP------DKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVH 74

                          90
                  ....*....|....*..
gi 213021190  315 QFPFHSAPALDVDWQNN 331
Cdd:pfam12894  75 HFSAGSDLITCLGWGEN 91
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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